ArticleExtremophiles : life under extreme conditions2008
The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination.
Article in Extremophiles : life under extreme conditions, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Role of RadA and DNA Polymerases in Recombination-Associated DNA Synthesis in Hyperthermophilic Archaea.Biomolecules · 2020Article
- Article
- Post-translational environmental switch of RadA activity by extein-intein interactions in protein splicing.Nucleic acids research · 2015Article
- Mediators of homologous DNA pairing.Cold Spring Harbor perspectives in biology · 2014Review
- Nanobiomotors of archaeal DNA repair machineries: current research status and application potential.Cell & bioscience · 2014Review
- Repair of DNA double-strand breaks following UV damage in three Sulfolobus solfataricus strains.Journal of bacteriology · 2010Article
- Structural and functional characterisation of a conserved archaeal RadA paralog with antirecombinase activity.Journal of molecular biology · 2009Article
- Article
- Genome analysis and genome-wide proteomics of Thermococcus gammatolerans, the most radioresistant organism known amongst the Archaea.Genome biology · 2009Article
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5 authors at 2 institutions in 1 country.
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Abstract
Archaea have recombination proteins similar to those of eukaryote, but many have not been characterized. Here, the characterization of a Rad55 homologue from Sulfolobus tokodaii (stRad55A) was reported. StRad55A protein preferred binding to ssDNA and had ssDNA-dependent ATPase activity. In addition, UV light could induce the expression of this protein, which was different from RadB, a RadA paralog found in euryarchaeota. Most importantly, stRad55A could release the suppression of excessive stSSB (single strand DNA binding protein from S. tokodaii) on the strand exchange catalyzed by stRadA (RadA homologue from S. tokodaii), by interacting directly with both stRadA and stSSB. StRad55A may function as a mediator to accelerate the displacement of stSSB by stRadA.
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